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Caveolae-associated protein 2 (Cavin-2) (Phosphatidylserine-binding protein) (Serum deprivation-response protein)

 CAVN2_MOUSE             Reviewed;         418 AA.
Q63918; Q3V1P6; Q78EC3; Q8CBT4;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
07-NOV-2018, entry version 127.
RecName: Full=Caveolae-associated protein 2;
AltName: Full=Cavin-2;
AltName: Full=Phosphatidylserine-binding protein;
AltName: Full=Serum deprivation-response protein;
Name=Cavin2;
Synonyms=Sdpr {ECO:0000312|MGI:MGI:99513},
Sdr {ECO:0000303|PubMed:8241023};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB28953.1}
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
PubMed=8241023;
Gustincich S., Schneider C.;
"Serum deprivation response gene is induced by serum starvation but
not by contact inhibition.";
Cell Growth Differ. 4:753-760(1993).
[2] {ECO:0000312|EMBL:BAC39116.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC39116.1};
TISSUE=Embryonic head {ECO:0000312|EMBL:BAE21104.1},
Embryonic spinal ganglion {ECO:0000312|EMBL:BAC39116.1}, and
Urinary bladder {ECO:0000312|EMBL:BAC29033.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3] {ECO:0000312|EMBL:AAH20008.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH27005.1}, and
FVB/N {ECO:0000312|EMBL:AAH20008.1};
TISSUE=Mammary gland {ECO:0000312|EMBL:AAH20008.1}, and
Retina {ECO:0000312|EMBL:AAH27005.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-293, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[5]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=18332105; DOI=10.1128/MCB.02186-07;
Ogata T., Ueyama T., Isodono K., Tagawa M., Takehara N., Kawashima T.,
Harada K., Takahashi T., Shioi T., Matsubara H., Oh H.;
"MURC, a muscle-restricted coiled-coil protein that modulates the
Rho/ROCK pathway, induces cardiac dysfunction and conduction
disturbance.";
Mol. Cell. Biol. 28:3424-3436(2008).
[6]
IDENTIFICATION IN THE CAVIN COMPLEX, INTERACTION WITH CAVIN1, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=19546242; DOI=10.1083/jcb.200903053;
Bastiani M., Liu L., Hill M.M., Jedrychowski M.P., Nixon S.J.,
Lo H.P., Abankwa D., Luetterforst R., Fernandez-Rojo M., Breen M.R.,
Gygi S.P., Vinten J., Walser P.J., North K.N., Hancock J.F.,
Pilch P.F., Parton R.G.;
"MURC/Cavin-4 and cavin family members form tissue-specific caveolar
complexes.";
J. Cell Biol. 185:1259-1273(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-293; SER-359
AND SER-363, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-35; SER-37;
SER-203; SER-204; SER-218; SER-283; SER-284; SER-287; SER-288;
SER-293; SER-296; SER-327; SER-336; SER-359; SER-363; THR-368; TYR-388
AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=23652019; DOI=10.1038/ncomms2808;
Hansen C.G., Shvets E., Howard G., Riento K., Nichols B.J.;
"Deletion of cavin genes reveals tissue-specific mechanisms for
morphogenesis of endothelial caveolae.";
Nat. Commun. 4:1831-1831(2013).
[10]
INTERACTION WITH CAVIN1.
PubMed=25588833; DOI=10.1242/jcs.161463;
Mohan J., Moren B., Larsson E., Holst M.R., Lundmark R.;
"Cavin3 interacts with cavin1 and caveolin1 to increase surface
dynamics of caveolae.";
J. Cell Sci. 128:979-991(2015).
-!- FUNCTION: Plays an important role in caveolar biogenesis and
morphology. Regulates caveolae morphology by inducing membrane
curvature within caveolae (By similarity). Plays a role in caveola
formation in a tissue-specific manner. Required for the formation
of caveolae in the lung and fat endothelia but not in the heart
endothelia. Negatively regulates the size or stability of CAVIN
complexes in the lung endothelial cells (PubMed:23652019). May
play a role in targeting PRKCA to caveolae (By similarity).
{ECO:0000250|UniProtKB:O95810, ECO:0000250|UniProtKB:Q66H98,
ECO:0000269|PubMed:23652019}.
-!- SUBUNIT: Component of the CAVIN complex composed of CAVIN1,
CAVIN2, CAVIN3 and CAVIN4 (PubMed:19546242). Binds to PRKCA in the
presence of phosphatidylserine. Interacts with CAVIN4; this
augments the transactivation of NPPA by CAVIN4 (By similarity).
Interacts with CAVIN1 (PubMed:25588833, PubMed:19546242).
Interacts with CAV3 (By similarity).
{ECO:0000250|UniProtKB:O95810, ECO:0000250|UniProtKB:Q66H98,
ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:25588833}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:19546242}.
Membrane, caveola {ECO:0000269|PubMed:19546242}. Note=Localizes in
the caveolae in a caveolin-dependent manner.
{ECO:0000269|PubMed:19546242}.
-!- TISSUE SPECIFICITY: Heart, adipose tissue, lung and endothelial
cells (at protein level). Highly expressed in kidney and expressed
at lower levels in liver, spleen, thymus, stomach, intestine and
uterus. {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:23652019,
ECO:0000269|PubMed:8241023}.
-!- DEVELOPMENTAL STAGE: Expression gradually increases during
embryonic stages and reaches a maximum in neonates.
{ECO:0000269|PubMed:18332105}.
-!- INDUCTION: Up-regulated in response to cardiac hypertrophy and in
serum-starved but not in density-dependent growth-arrested NIH3T3
cells. Down-regulated within 6 hours after the addition of serum
or epidermal growth factor to serum-starved cells.
{ECO:0000269|PubMed:18332105, ECO:0000269|PubMed:8241023}.
-!- DOMAIN: The leucine-zipper domain is essential for its
localization in the caveolae. {ECO:0000250|UniProtKB:O95810}.
-!- PTM: The N-terminus is blocked. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show loss of endothelial caveolae in
lung and adipose tissue but no effect on the abundance of
endothelial caveolae in the heart. {ECO:0000269|PubMed:23652019}.
-!- MISCELLANEOUS: Binds phosphatidylserine (PS) in a calcium-
independent manner. PS-binding is inhibited by phosphotidic acid
and phosphatidylinositol. Does not bind phosphatidylcholine (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the CAVIN family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S67386; AAB28953.1; -; mRNA.
EMBL; AK035324; BAC29033.1; -; mRNA.
EMBL; AK084096; BAC39116.1; -; mRNA.
EMBL; AK132324; BAE21104.1; -; mRNA.
EMBL; BC020008; AAH20008.1; -; mRNA.
EMBL; BC027005; AAH27005.1; -; mRNA.
CCDS; CCDS14940.1; -.
RefSeq; NP_620080.1; NM_138741.1.
UniGene; Mm.398690; -.
ProteinModelPortal; Q63918; -.
SMR; Q63918; -.
IntAct; Q63918; 3.
MINT; Q63918; -.
STRING; 10090.ENSMUSP00000055694; -.
iPTMnet; Q63918; -.
PhosphoSitePlus; Q63918; -.
SwissPalm; Q63918; -.
MaxQB; Q63918; -.
PaxDb; Q63918; -.
PeptideAtlas; Q63918; -.
PRIDE; Q63918; -.
Ensembl; ENSMUST00000051572; ENSMUSP00000055694; ENSMUSG00000045954.
GeneID; 20324; -.
KEGG; mmu:20324; -.
UCSC; uc007axk.1; mouse.
CTD; 8436; -.
MGI; MGI:99513; Cavin2.
eggNOG; ENOG410IEZA; Eukaryota.
eggNOG; ENOG410XP8W; LUCA.
GeneTree; ENSGT00530000063058; -.
HOGENOM; HOG000293135; -.
HOVERGEN; HBG056807; -.
InParanoid; Q63918; -.
OMA; GSDMRQE; -.
OrthoDB; EOG091G09Y1; -.
PhylomeDB; Q63918; -.
TreeFam; TF331031; -.
ChiTaRS; Sdpr; mouse.
PRO; PR:Q63918; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000045954; Expressed in 267 organ(s), highest expression level in right lung.
CleanEx; MM_SDPR; -.
Genevisible; Q63918; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0005901; C:caveola; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
InterPro; IPR033298; Cavin2.
InterPro; IPR026752; Cavin_fam.
PANTHER; PTHR15240; PTHR15240; 1.
PANTHER; PTHR15240:SF1; PTHR15240:SF1; 1.
Pfam; PF15237; PTRF_SDPR; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Lipid-binding;
Membrane; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O95810}.
CHAIN 2 418 Caveolae-associated protein 2.
/FTId=PRO_0000238919.
REGION 2 168 Interaction with CAVIN1.
{ECO:0000269|PubMed:25588833}.
REGION 62 100 Leucine-zipper.
{ECO:0000250|UniProtKB:O95810}.
COILED 61 87 {ECO:0000255}.
COILED 126 268 {ECO:0000255}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:O95810}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 51 51 Phosphoserine.
{ECO:0000250|UniProtKB:Q66H98}.
MOD_RES 196 196 Phosphothreonine.
{ECO:0000250|UniProtKB:O95810}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 368 368 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 388 388 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000250|UniProtKB:Q66H98}.
CONFLICT 14 14 P -> L (in Ref. 2; BAE21104).
{ECO:0000305}.
CONFLICT 76 76 Q -> L (in Ref. 2; BAC29033).
{ECO:0000305}.
CONFLICT 173 173 K -> R (in Ref. 2; BAC29033).
{ECO:0000305}.
SEQUENCE 418 AA; 46764 MW; EFD7B4E383785F41 CRC64;
MGEDAAQAEK FQHPNTDMLQ EKPSSPSPMP SSTPSPSLNL GSTEEAIRDN SQVNAVTVHT
LLDKLVNMLD AVRENQHNME QRQINLEGSV KGIQNDLTKL SKYQASTSNT VSKLLEKSRK
VSAHTRAVRE RLERQCVQVK RLENNHAQLL RRNHFKVLIF QEESEIPASV FVKEPVPSAA
EGKEELADEN KSLEETLHNV DLSSDDELPR DEEALEDSAE EKMEESRAEK IKRSSLKKVD
SLKKAFSRQN IEKKMNKLGT KIVSVERREK IKKSLTPNHQ KASSGKSSPF KVSPLSFGRK
KVREGESSVE NETKLEDQMQ EDREEGSFTE GLSEASLPSG LMEGSAEDAE KSARRGNNSA
VGSNADLTIE EDEEEEPVAL QQAQQVRYES GYMLNSEEME EPSEKQVQPA VLHVDQTA


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